Analytical Data
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Gene name
KLRG1
- Application
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Alternative Names
KLRG1;CLEC15A;MAFA;MAFAL;Killer cell lectin-like receptor subfamily G member 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96E93-2
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Expression Region
60-189aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSLCQGSNYSTCASCPSCPDRWMKYGNHC YYFSVEEKDWNSSLEFCLARDSHLLVITDNQEMSLLQVFLSEAFCWIGLR NNSGWRWEDGSPLNFSRISSNSFVQTCGAINKNGLQASSCEVPLHWVCKK VRL
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Molecular Weight
17 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
KLRG1 (Killer Cell Lectin-Like Receptor G1) is an inhibitory receptor primarily expressed on natural killer (NK) cells and certain T cell subsets, playing a crucial role in regulating immune responses. Its function is primarily associated with the regulation of immune cell activity, particularly in controlling the proliferation and effector functions of lymphocytes. Research has increasingly focused on KLRG1 due to its potential as a biomarker for immune system status, particularly in tumors and chronic infections. KLRG1 expression is often upregulated in exhausted T cells, indicating a state of functional decline, which is a major concern in cancer immunotherapy. The study of KLRG1, particularly in the context of recombinant protein technology, aims to elucidate its role in immune modulation and to explore therapeutic strategies that could enhance anti-tumor immunity. Recombinant KLRG1 proteins can be used to identify binding partners, study signaling pathways, and evaluate their impact on NK and T cell functions. Moreover, understanding the structural and functional aspects of KLRG1 can lead to the development of novel immune-therapeutic agents aimed at rejuvenating exhausted T cells or manipulating NK cell activity for improved cancer treatment outcomes. Thus, KLRG1 recombinant proteins serve as an essential tool in immune research, providing insights that could inform innovative strategies against various diseases, particularly malignancies and persistent viral infections.
